Abstract
The modular assembly of synthetic transhydrogenase catalysts is demonstrated using a PEG-NAD(H) modified formate dehydrogenase (FDH)-SpyCatcher fusion protein. The front cover highlights how any oxidoreductase enzyme can be outfitted with a simple SpyTag peptide and conjugated to FDH-SpyCatcher to create new cofactor-independent biocatalysts driven by formate oxidation. The stabilities and catalytic properties of the resulting transhydrogenases are improved without detriment to the selectivities of the native active sites, emphasizing the functional modularity and predictive nature of this synthetic approach to biocatalyst design. More information can be found in the Full Paper by N. Massad and S. Banta.
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